A transforming mutation in the pleckstrin homology domain of AKT1 in cancer (Q27646556)

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Andrew L Faber

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Candice Horn

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Gregory P Donoho

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Stephen L Briggs

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Christiane M Robbins

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Galen Hostetter

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Sophie Boguslawski

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Tracy Y Moses

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Stephanie Savage

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Mark Uhlik

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Aimin Lin

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Jian Du

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Yue-Wei Qian

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Douglas J Zeckner

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Jeffrey Touchman

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Ketan Patel

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Spyro Mousses

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Michael Bittner

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Richard Schevitz

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Mei-Huei T Lai

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Kerry L Blanchard

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James E Thomas

AKT1/PKBalpha kinase is frequently elevated in human cancers and its constitutive activation is required for oncogenic transformation in NIH3T3 cells

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language of work or name

English

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publication date

26 July 2007

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published in

Nature

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volume

448

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issue

7152

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page(s)

439-44

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cites work

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A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain.

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The phosphatidylinositol 3-Kinase AKT pathway in human cancer

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The PIK3CA gene is mutated with high frequency in human breast cancers.

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Mutation of the PIK3CA gene in ovarian and breast cancer

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PIK3CA gene is frequently mutated in breast carcinomas and hepatocellular carcinomas.

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Frequent mutation of the PIK3CA gene in ovarian and breast cancers

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PIK3CA mutations correlate with hormone receptors, node metastasis, and ERBB2, and are mutually exclusive with PTEN loss in human breast carcinoma

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High frequency of mutations of the PIK3CA gene in human cancers

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New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway

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PTEN promoter is methylated in a proportion of invasive breast cancers

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The phosphoinositide 3-kinase pathway

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Living with lethal PIP3 levels: viability of flies lacking PTEN restored by a PH domain mutation in Akt/PKB.

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Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1,3,4,5-tetrakisphosphate binding capacity

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The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase

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Transformation potential of Ras isoforms correlates with activation of phosphatidylinositol 3-kinase but not ERK.

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Role of translocation in the activation and function of protein kinase B

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The consensus coding sequences of human breast and colorectal cancers

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Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change

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High-resolution structure of the pleckstrin homology domain of protein kinase b/akt bound to phosphatidylinositol (3,4,5)-trisphosphate

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Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphates.

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Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate

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Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B

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Identification and characterization of pleckstrin-homology-domain-dependent and isoenzyme-specific Akt inhibitors

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Akt/PKB localisation and 3' phosphoinositide generation at sites of epithelial cell-matrix and cell-cell interaction

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Multiple phosphoinositide 3-kinase-dependent steps in activation of protein kinase B

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The c-myc oncogene driven by immunoglobulin enhancers induces lymphoid malignancy in transgenic mice

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Survival signalling by Akt and eIF4E in oncogenesis and cancer therapy

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Perturbations of the AKT signaling pathway in human cancer

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Colorectal cancer: mutations in a signalling pathway

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Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: amplification of AKT1 in a primary human gastric adenocarcinoma

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Genetic alterations and aberrant expression of genes related to the phosphatidyl-inositol-3'-kinase/protein kinase B (Akt) signal transduction pathway in glioblastomas.

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Mutational analysis of AKT1, AKT2 and AKT3 genes in common human carcinomas

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